未折叠蛋白质的普遍初始热力学亚稳态  

Universal Initial Thermodynamic Metastable State of Unfolded Proteins

作　　者：杨霖[1,2] 郭帅 马晓亮[1] 侯成宇[3] 史丽萍[1] 李佳成[1] 赫晓东[1] YANG Lin;GUO Shuai;MAXiao-Liang;HOU Cheng-Yu;SHI Li-Ping;LI Jia-Cheng;HE Xiao-Dong(National Key Laboratory of Science and Technology on Advanced Composites in Special Environments,Harbin Institute of Technology,Harbin 150080,China;School of Aerospace,Mechanical and Mechatronic Engineering,The University of Sydney,NSW 2006,Australia;School of Electronics and Information Engineering,Harbin Institute of Technology,Harbin 150080,China)

机构地区：[1]哈尔滨工业大学特种环境复合材料技术国家级重点实验室,哈尔滨150080 [2]School of Aerospace,Mechanical and Mechatronic Engineering,The University of Sydney,NSW 2006,Australia [3]哈尔滨工业大学电子与信息工程学院,哈尔滨150080

出　　处：《生物化学与生物物理进展》2019年第10期993-1001,共9页Progress In Biochemistry and Biophysics

基　　金：中央高校基本科研专项资金;深圳市科技计划资助项目~~

摘　　要：探索和理解蛋白质折叠问题一直是分子生物学、结构生物学和生物物理学的终极挑战.未折叠的蛋白质应该存在一种普遍初始热力学亚稳态,否则无法解释蛋白质是如何在剧烈的热振动干扰下完成快速精确折叠的.本文通过分析水溶液环境和蛋白质折叠的相关性,揭示了一种由水分子屏蔽效应引起的未折叠蛋白质的普遍初始热力学亚稳态,该亚稳态的存在是水溶液环境中水分子的物理性质决定,并赋予未折叠蛋白质抵抗热扰动和避免错误折叠的能力.我们通过研究已发表的实验数据和建立分子模型,找到了该初始热力学亚稳态存在的相关证据,并推测了该亚稳态导致蛋白质精确折叠的相关物理学机制.Understanding and explaining how proteins fold have been the ultimate challenges in molecular and structure biology. Protein folding should initiate from a thermodynamic metastable state of unfolded proteins,otherwise, it is difficult to explain how an unfolded protein chain folds exactly into its native 3 D structure in an expeditious and reproducible manner under severe thermal disturbance from temperature. Considering dependency of protein folding on aqueous environments and unique physical properties of water molecules, this study uncovers an initial thermodynamic metastable state of unfolded proteins in aqueous environment that enables them to that resists thermal-motion and avoids misfolding. The existence of the thermodynamic metastable state of unfolded proteins are verified by analyzing the results available from experiments in the literature. The principles of physics are applied to estimate the breakage of the thermodynamic metastable state of specific amino acids, that enable the leading to the inferred as physical folding mechanisms and codes for proteins.

关 键 词：未折叠蛋白质 蛋白质二级结构 水分子屏蔽效应 热力学亚稳态 

分 类 号：Q71[生物学—分子生物学]